EC |
5.4.99.58 |
Accepted name: |
methylornithine synthase |
Reaction: |
L-lysine = (3R)-3-methyl-D-ornithine |
Glossary: |
(3R)-3-methyl-D-ornithine = (2R,3R)-2,5-diamino-3-methylpentanoate |
Other name(s): |
PylB |
Systematic name: |
L-lysine carboxy-aminomethylmutase |
Comments: |
The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182] |
2. |
Quitterer, F., List, A., Eisenreich, W., Bacher, A. and Groll, M. Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis. Angew. Chem. Int. Ed. Engl. 51 (2012) 1339–1342. [DOI] [PMID: 22095926] |
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[EC 5.4.99.58 created 2012] |
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EC |
6.3.2.59 |
Accepted name: |
3-methyl-D-ornithine—L-lysine ligase |
Reaction: |
ATP + (3R)-3-methyl-D-ornithine + L-lysine = ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine |
Glossary: |
L-pyrrolysine = N6-{[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl}-L-lysine |
Other name(s): |
N6-[(2R,3R)-3-methylornithyl]-L-lysine synthase; 3-methylornithine—L-lysine ligase; pylC (gene name) |
Systematic name: |
(3R)-3-methyl-D-ornithine:L-lysine γ-ligase (ADP-forming) |
Comments: |
The enzyme participates in the biosynthesis of L-pyrrolysine, a naturally occurring, genetically coded amino acid found in some methanogenic archaea and a few bacterial species. L-pyrrolysine is present in several methyltransferases that are involved in methyl transfer from methylated amine compounds to coenzyme M. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182] |
2. |
Cellitti, S.E., Ou, W., Chiu, H.P., Grunewald, J., Jones, D.H., Hao, X., Fan, Q., Quinn, L.L., Ng, K., Anfora, A.T., Lesley, S.A., Uno, T., Brock, A. and Geierstanger, B.H. D-Ornithine coopts pyrrolysine biosynthesis to make and insert pyrroline-carboxy-lysine. Nat. Chem. Biol. 7 (2011) 528–530. [DOI] [PMID: 21525873] |
3. |
Quitterer, F., List, A., Beck, P., Bacher, A. and Groll, M. Biosynthesis of the 22nd genetically encoded amino acid pyrrolysine: structure and reaction mechanism of PylC at 1.5A resolution. J. Mol. Biol. 424 (2012) 270–282. [DOI] [PMID: 22985965] |
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[EC 6.3.2.59 created 2021] |
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